1FNY
LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.
Summary for 1FNY
| Entry DOI | 10.2210/pdb1fny/pdb |
| Related | 1FNZ |
| Descriptor | BARK AGGLUTININ I,POLYPEPTIDE A, CALCIUM ION (3 entities in total) |
| Functional Keywords | legume lectin, jelly roll, sugar binding protein |
| Biological source | Robinia pseudoacacia |
| Total number of polymer chains | 1 |
| Total formula weight | 25650.68 |
| Authors | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J. (deposition date: 2000-08-24, release date: 2001-08-24, Last modification date: 2024-03-13) |
| Primary citation | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J. Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine. Proteins, 44:470-478, 2001 Cited by PubMed Abstract: The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N-acetylgalactosamine. The free form is refined at 1.80 A resolution to an R-factor of 18.9% whereas the complexed structure has an R-factor of 19.7% at 2.05 A resolution. Both structures are compared to each other and to other available legume lectin structures. The polypeptide chains of the two structures exhibit the characteristic legume lectin tertiary fold. The quaternary structure resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features leading to the extreme stability of this lectin. PubMed: 11484224DOI: 10.1002/prot.1112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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